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UniProtKB/Swiss-Prot entry Q9MUR4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPB_MESVI
Primary accession number Q9MUR4
Secondary accession numbers None
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 42)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta
Synonym EC 1.2.4.1
Gene name
Name: pdhB
Synonyms: odpB
From
Mesostigma viride [TaxID: 41882] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae; Mesostigmatales; Mesostigmataceae; Mesostigma.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NIES-296;
DOI=10.1038/35001059; PubMed=10688199 [NCBI, ExPASy, EBI, Israel, Japan]
Lemieux C., Otis C., Turmel M.;
"Ancestral chloroplast genome in Mesostigma viride reveals an early branch of green plant evolution.";
Nature 403:649-652(2000).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
  • SUBCELLULAR LOCATION: Plastid, chloroplast.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF166114; AAF43837.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_038396.1; -.
3D structure databases
HSSP Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]
ModBase Q9MUR4.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS Q9MUR4.
Genome annotation databases
GeneID 800962; -.
Other
ProtoNet Q9MUR4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   327  327     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000162218
BINDING   60    60        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 36005 Da [This is the MW of the unprocessed precursor] CRC64: 8E8D7CD1ADD64E5A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVRFLFEAL NMAIDEEMAR NDKVALLGED IGHYGGSYKV TQNLYAKYGE HRVIDTPIAE 

        70         80         90        100        110        120 
NSFVGAAIGA AMTGLVTVVE GMNMGFILLA FSQISNNMGM LSATSGGHYH IPIVLRGPGG 

       130        140        150        160        170        180 
VGKQLGAEHS QRLECYFQSV PGLQIVACST PYNAKGLLKS AIRSKNPIFF LEHVLLYNLK 

       190        200        210        220        230        240 
AEVPDNDYVL PLEKAEIVRQ GNDITILTYS RMRYNVIQAV KVLVEKGYDP EIIDLISLKP 

       250        260        270        280        290        300 
FDIETIGKSI QKTHKVLIVE ESMMTGGISN VLQSLILENF FDDLDNRPMC LSSPNVPTPY 

       310        320 
SGPLEEVSIV QTADIIESVE QILTNKM 

Q9MUR4 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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